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PDBsum entry 4ilx

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Lyase/lyase inhibitor PDB id
4ilx
Jmol
Contents
Protein chain
257 a.a.
Ligands
GOL ×2
1EZ
DMS
Metals
_ZN
Waters ×261
HEADER    LYASE/LYASE INHIBITOR                   01-JAN-13   4ILX
TITLE     STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH AN ADAMANTYL
TITLE    2 SULFONAMIDE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND   5 CARBONIC ANHYDRASE II, CA-II;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET VECTOR
KEYWDS    LYASE, REVERSIBLE HYDRATION OF CARBON DIOXIDE, CYTOSOLIC, LYASE-LYASE
KEYWDS   2 INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.BISWAS,R.MCKENNA
REVDAT   2   29-MAY-13 4ILX    1       JRNL
REVDAT   1   13-FEB-13 4ILX    0
JRNL        AUTH   S.BISWAS,F.CARTA,A.SCOZZAFAVA,R.MCKENNA,C.T.SUPURAN
JRNL        TITL   STRUCTURAL EFFECT OF PHENYL RING COMPARED TO THIADIAZOLE
JRNL        TITL 2 BASED ADAMANTYL-SULFONAMIDES ON CARBONIC ANHYDRASE
JRNL        TITL 3 INHIBITION.
JRNL        REF    BIOORG.MED.CHEM.              V.  21  2314 2013
JRNL        REFN                   ISSN 0968-0896
JRNL        PMID   23490152
JRNL        DOI    10.1016/J.BMC.2013.02.022
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.70
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.7
REMARK   3   NUMBER OF REFLECTIONS             : 29545
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150
REMARK   3   R VALUE            (WORKING SET) : 0.149
REMARK   3   FREE R VALUE                     : 0.185
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1506
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 26.7028 -  3.5553    0.95     2713   168  0.1601 0.1996
REMARK   3     2  3.5553 -  2.8230    0.96     2692   127  0.1467 0.1774
REMARK   3     3  2.8230 -  2.4664    0.95     2660   137  0.1558 0.1857
REMARK   3     4  2.4664 -  2.2410    0.94     2609   137  0.1476 0.1719
REMARK   3     5  2.2410 -  2.0805    0.93     2558   149  0.1433 0.1790
REMARK   3     6  2.0805 -  1.9579    0.92     2558   123  0.1384 0.1563
REMARK   3     7  1.9579 -  1.8598    0.91     2502   140  0.1359 0.1841
REMARK   3     8  1.8598 -  1.7789    0.90     2484   135  0.1390 0.1967
REMARK   3     9  1.7789 -  1.7104    0.89     2432   143  0.1460 0.1934
REMARK   3    10  1.7104 -  1.6514    0.88     2432   131  0.1418 0.1836
REMARK   3    11  1.6514 -  1.6000    0.87     2399   116  0.1436 0.1957
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.400
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.006           2255
REMARK   3   ANGLE     :  1.135           3089
REMARK   3   CHIRALITY :  0.079            324
REMARK   3   PLANARITY :  0.005            401
REMARK   3   DIHEDRAL  : 16.324            855
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4ILX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB076917.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5
REMARK 200  MONOCHROMATOR                  : VARIMAX OPTICS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.1
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM CITRATE TRIS BUFFER PH
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       20.67700
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OE2  GLU A   214     O    HOH A   575              2.07
REMARK 500   OE1  GLN A   136     O    HOH A   563              2.12
REMARK 500   OD2  ASP A    85     O    HOH A   618              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   638     O    HOH A   643     2555     2.17
REMARK 500   O    HOH A   526     O    HOH A   555     1655     2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLU A 234   OE1 -  CD  -  OE2 ANGL. DEV. = -123.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LYS A 111       -1.26     72.45
REMARK 500    ASN A 244       49.44    -94.51
REMARK 500    LYS A 252     -138.36     54.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 103.5
REMARK 620 3 HIS A 119   ND1 111.2  97.4
REMARK 620 4 1EZ A 303   N01 113.6 112.6 116.7
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EZ A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 305
DBREF  4ILX A    4   261  UNP    P00918   CAH2_HUMAN       4    260
SEQRES   1 A  257  HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS TRP
SEQRES   2 A  257  HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN SER
SEQRES   3 A  257  PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP PRO
SEQRES   4 A  257  SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA THR
SEQRES   5 A  257  SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN VAL
SEQRES   6 A  257  GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS GLY
SEQRES   7 A  257  GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE HIS
SEQRES   8 A  257  PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU HIS
SEQRES   9 A  257  THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS LEU
SEQRES  10 A  257  VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS ALA
SEQRES  11 A  257  VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE PHE
SEQRES  12 A  257  LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS VAL
SEQRES  13 A  257  VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS SER
SEQRES  14 A  257  ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU PRO
SEQRES  15 A  257  GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU THR
SEQRES  16 A  257  THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL LEU
SEQRES  17 A  257  LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU LYS
SEQRES  18 A  257  PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO GLU
SEQRES  19 A  257  GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO LEU
SEQRES  20 A  257  LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 301       1
HET    GOL  A 302       6
HET    1EZ  A 303      24
HET    GOL  A 304       6
HET    DMS  A 305       4
HETNAM      ZN ZINC ION
HETNAM     GOL GLYCEROL
HETNAM     1EZ N-(4-SULFAMOYLPHENYL)-2-[(3S,5S,7S)-TRICYCLO[3.3.1.1~3,
HETNAM   2 1EZ  7~]DEC-1-YL]ACETAMIDE
HETNAM     DMS DIMETHYL SULFOXIDE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  GOL    2(C3 H8 O3)
FORMUL   4  1EZ    C18 H24 N2 O3 S
FORMUL   6  DMS    C2 H6 O S
FORMUL   7  HOH   *257(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  LEU A 212
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  LYS A  80   N  SER A  48
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK         NE2 HIS A  94                ZN    ZN A 301     1555   1555  1.99
LINK         NE2 HIS A  96                ZN    ZN A 301     1555   1555  2.02
LINK         ND1 HIS A 119                ZN    ZN A 301     1555   1555  2.08
LINK        ZN    ZN A 301                 N01 1EZ A 303     1555   1555  1.92
CISPEP   1 SER A   29    PRO A   30          0        -1.17
CISPEP   2 PRO A  201    PRO A  202          0         8.30
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  1EZ A 303
SITE     1 AC2 10 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC2 10 GLN A  92  HIS A  94  1EZ A 303  HOH A 421
SITE     3 AC2 10 HOH A 440  HOH A 472
SITE     1 AC3 13 HIS A  94  HIS A  96  HIS A 119  PHE A 131
SITE     2 AC3 13 VAL A 135  LEU A 198  THR A 199  THR A 200
SITE     3 AC3 13 TRP A 209   ZN A 301  GOL A 302  HOH A 455
SITE     4 AC3 13 HOH A 608
SITE     1 AC4  8 LEU A 164  ASP A 165  LYS A 168  LYS A 225
SITE     2 AC4  8 LYS A 228  LEU A 229  HOH A 532  HOH A 635
SITE     1 AC5  3 TYR A   7  ASP A 243  TRP A 245
CRYST1   42.382   41.354   72.096  90.00 104.10  90.00 P 1 21 1      2
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.023595  0.000000  0.005926        0.00000
SCALE2      0.000000  0.024181  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014301        0.00000
      
PROCHECK
Go to PROCHECK summary
 References